Hackett C J, Askonas B A
Immunology. 1982 Mar;45(3):431-8.
The proximity of H-2K and D antigens and influenza virus haemagglutinin (HA) molecules on the surface of infected target cells was assessed by a topographical study using monoclonal antibodies to H-2 and to HA. The effect of pretreatment of fixed, infected cells with excess of one monoclonal antibody on the subsequent binding of a second radiolabelled antibody was measured. Using CBA mouse B lymphoblasts which were paraformaldehyde fixed 5 hr postinfection with influenza virus (A/USSR/90/77), pretreatment with monoclonal antibody 30/3 to H-2Kk and Dk partially blocked (Approximately equal to 37%) the binding of one radiolabelled monoclonal anti-HA antibody (264/2). A different monoclonal IgG (W18/1) directed to the same HA molecule was not blocked by similar pretreatment of cells with the anti-H-2 antibody. Interaction of monoclonal antibodies with their sites is highly specific, and mutual blocking of two antibodies requires very closely located sites even if the antibodies are directed to the same molecule. We therefore have evidence for proximity of H-2 and HA molecules; however, we were unable to demonstrate cocapping of H-2K and D antigens with influenza HA.
利用针对H-2和流感病毒血凝素(HA)的单克隆抗体,通过一项拓扑学研究评估了感染的靶细胞表面H-2K和D抗原与流感病毒血凝素(HA)分子的接近程度。测定了用过量一种单克隆抗体对固定的感染细胞进行预处理后,对随后第二种放射性标记抗体结合的影响。使用感染流感病毒(A/USSR/90/77)5小时后用多聚甲醛固定的CBA小鼠B淋巴母细胞,用针对H-2Kk和Dk的单克隆抗体30/3进行预处理,部分阻断(约37%)了一种放射性标记的单克隆抗HA抗体(264/2)的结合。针对同一HA分子的另一种单克隆IgG(W18/1),在用抗H-2抗体对细胞进行类似预处理时未被阻断。单克隆抗体与其位点的相互作用具有高度特异性,两种抗体的相互阻断需要位点非常紧密地定位,即使抗体针对的是同一分子。因此,我们有证据表明H-2和HA分子接近;然而,我们无法证明H-2K和D抗原与流感HA共帽。